Lipid acyl hydrolase of patatin
- 1 August 1984
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Botany
- Vol. 62 (8) , 1640-1644
- https://doi.org/10.1139/b84-220
Abstract
Patatin, the major protein of potato tubers, was copurified with lipid acyl hydrolase (LAH). The common identity of LAH and patatin was demonstrated by sodium dodecyl sulfate denaturation studies, isoelectric focusing and the inhibition of LAH activity by patatin antiserum.This publication has 6 references indexed in Scilit:
- Analysis of the Heterogeneity of the 40,000 Molecular Weight Tuber Glycoprotein of Potatoes by Immunological Methods and by NH2-Terminal Sequence AnalysisPlant Physiology, 1983
- Induction and Accumulation of Major Tuber Proteins of Potato in Stems and PetiolesPlant Physiology, 1983
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Esterase isozymes from Solanum tubersPhytochemistry, 1967
- Disc electrophoresis of tuber proteins from Solanum species and interspecific hybridsPhytochemistry, 1966
- A study of some plant esterasesPhytochemistry, 1964